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Originally published In Press as doi:10.1074/jbc.M103162200 on April 19, 2001

J. Biol. Chem., Vol. 276, Issue 26, 23456-23463, June 29, 2001
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Human Intelectin Is a Novel Soluble Lectin That Recognizes Galactofuranose in Carbohydrate Chains of Bacterial Cell Wall*

Shoutaro TsujiDagger §, Junji UehoriDagger , Misako MatsumotoDagger §, Yasuhiko Suzuki, Akio Matsuhisa||, Kumao ToyoshimaDagger , and Tsukasa SeyaDagger §**

From the Dagger  Department of Immunology, Osaka Medical Center for Cancer and Cardiovascular Diseases, Higashinari-ku, Osaka 537-8511, the  Osaka Prefectural Institute of Public Health, Higashinari-ku, Osaka 537-0025, the || Research and Development Center, Fuso Pharmaceutical Industries, Ltd., Joto-ku, Osaka 536-8523, and the § Organization for Pharmaceutical Safety and Research, Tokyo 100-0013, Japan

Galactofuranosyl residues are present in various microorganisms but not in mammals. In this study, we identified a human lectin binding to galactofuranosyl residues and named this protein human intelectin (hIntL). The mature hIntL was a secretory glycoprotein consisting of 295 amino acids and N-linked oligosaccharides, and its basic structural unit was a 120-kDa homotrimer in which 40-kDa polypeptides were bridged by disulfide bonds. The hIntL gene was split into 8 exons on chromosome 1q21.3, and hIntL mRNA was expressed in the heart, small intestine, colon, and thymus. hIntL showed high levels of homology with mouse intelectin, Xenopus laevis cortical granule lectin/oocyte lectin, lamprey serum lectin, and ascidian galactose-specific lectin. These homologues commonly contained no carbohydrate recognition domain, which is a characteristic of C-type lectins, although some of them have been reported as Ca2+-dependent lectins. Recombinant hIntL revealed affinities to D-pentoses and a D-galactofuranosyl residue in the presence of Ca2+, and recognized the bacterial arabinogalactan of Nocardia containing D-galactofuranosyl residues. These results suggested that hIntL is a new type lectin recognizing galactofuranose, and that hIntL plays a role in the recognition of bacteria-specific components in the host.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AB036706.

** To whom correspondence should be addressed: Dept. of Immunology, Osaka Medical Center for Cancer and Cardiovascular Diseases, Higashinari-ku, Osaka 537-8511, Japan. Tel./Fax: 81-6-6973-1209; E-mail: tseya@mail.mc.pref.osaka.jp.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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